Investigating the Ligand-Binding Properties of N-arylbenzimidazoles as Novel Elastase Inhibitors.

ABSTRACT: Human elastase 1 has been shown to possess an important role in maintaining skin stability and elasticity through the proteolytic cleavage of elastin (ELN), a hydrophobic protein that serves as a key component of extracellular matrix in the skin. The development of antielastase agents represents a promising therapeutic approach for treating skin pathologies characterized by elastin degradation, with applications in both dermatology and cosmetology. Reversible inhibitors represent a therapeutic strategy, offering selective inhibition of elastase proteolytic activity while preserving the function of other physiologically essential serine proteases. Using porcine pancreatic elastase (PPE) as a well-established surrogate of human skin elastase, a focused series of noncovalent inhibitors design

SUBMITTER: Pitasi G 

PROVIDER: S-EPMC12913230 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature